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O00086

- IMDH_CANAX

UniProt

O00086 - IMDH_CANAX

Protein

Inosine-5'-monophosphate dehydrogenase

Gene

IMH3

Organism
Candida albicans (Yeast)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 1 (01 Jul 1997)
      Previous versions | rss
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    Functioni

    Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth.1 PublicationUniRule annotation

    Catalytic activityi

    Inosine 5'-phosphate + NAD+ + H2O = xanthosine 5'-phosphate + NADH.UniRule annotation

    Cofactori

    Potassium.UniRule annotation

    Enzyme regulationi

    Mycophenolic acid (MPA) is a non-competitive inhibitor that prevents formation of the closed enzyme conformation by binding to the same site as the amobile flap. In contrast, mizoribine monophosphate (MZP) is a competitive inhibitor that induces the closed conformation. MPA is a potent inhibitor of mammalian IMPDHs but a poor inhibitor of the bacterial enzymes. MZP is a more potent inhibitor of bacterial IMPDH. Potently inhibited by MPA.1 PublicationUniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi328 – 3281Potassium; via carbonyl oxygenUniRule annotation
    Metal bindingi330 – 3301Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei331 – 3311IMPUniRule annotation
    Active sitei333 – 3331Thioimidate intermediateUniRule annotation
    Metal bindingi333 – 3331Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei447 – 4471IMPUniRule annotation
    Metal bindingi506 – 5061Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
    Metal bindingi507 – 5071Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
    Metal bindingi508 – 5081Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi276 – 2783NADUniRule annotation
    Nucleotide bindingi326 – 3283NADUniRule annotation

    GO - Molecular functioni

    1. adenyl nucleotide binding Source: InterPro
    2. IMP dehydrogenase activity Source: UniProtKB-HAMAP
    3. metal ion binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. GMP biosynthetic process Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    GMP biosynthesis, Purine biosynthesis

    Keywords - Ligandi

    Metal-binding, NAD, Potassium

    Enzyme and pathway databases

    UniPathwayiUPA00601; UER00295.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Inosine-5'-monophosphate dehydrogenaseUniRule annotation (EC:1.1.1.205UniRule annotation)
    Short name:
    IMP dehydrogenaseUniRule annotation
    Short name:
    IMPDUniRule annotation
    Short name:
    IMPDHUniRule annotation
    Gene namesi
    Name:IMH3
    Synonyms:IMD3
    OrganismiCandida albicans (Yeast)
    Taxonomic identifieri5476 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

    Organism-specific databases

    CGDiCAL0000509. IMH3.

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 521521Inosine-5'-monophosphate dehydrogenasePRO_0000093685Add
    BLAST

    2D gel databases

    COMPLUYEAST-2DPAGEO00086.

    Expressioni

    Developmental stagei

    Expressed at equal levels in the yeast or hyphal form.

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    STRINGi5476.CAL0000509.

    Structurei

    3D structure databases

    ProteinModelPortaliO00086.
    SMRiO00086. Positions 9-519.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini119 – 17860CBS 1UniRule annotationAdd
    BLAST
    Domaini182 – 23857CBS 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni366 – 3683IMP bindingUniRule annotation
    Regioni389 – 3902IMP bindingUniRule annotation
    Regioni413 – 4175IMP bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the IMPDH/GMPR family.UniRule annotation
    Contains 2 CBS domains.UniRule annotation

    Keywords - Domaini

    CBS domain, Repeat

    Phylogenomic databases

    eggNOGiCOG0517.
    PhylomeDBiO00086.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_01964. IMPDH.
    InterProiIPR013785. Aldolase_TIM.
    IPR000644. CBS_dom.
    IPR005990. IMP_DH.
    IPR015875. IMP_DH/GMP_Rdtase_CS.
    IPR001093. IMP_DH_GMPRt.
    [Graphical view]
    PANTHERiPTHR11911:SF6. PTHR11911:SF6. 1 hit.
    PfamiPF00571. CBS. 2 hits.
    PF00478. IMPDH. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000130. IMPDH. 1 hit.
    SMARTiSM00116. CBS. 2 hits.
    [Graphical view]
    TIGRFAMsiTIGR01302. IMP_dehydrog. 1 hit.
    PROSITEiPS51371. CBS. 2 hits.
    PS00487. IMP_DH_GMP_RED. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O00086-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVFETSKATS YLKDYPKKDG LSVKELIDST NFGGLTYNDF LILPGLINFP    50
    SSAVSLETKL TKKITLKSPF VSSPMDTVTE ENMAIHMALL GGIGIIHHNC 100
    TSEEQAEMVR KVKKYENGFI NDPVVISPEV TVGEVKKMGE VLGFTSFPVT 150
    ENGKVGGKLV GIITSRDIQF HEDNKSPVSE VMTKDLVVGK KGISLTDGNE 200
    LLRSSKKGKL PIVDAEGNLV SLISRTDLQK NQDYPNASKS FHSKQLLCGA 250
    AIGTIDADRE RLDKLVEAGL DVVVLDSSNG SSVFQLNMIK WIKEKYPELQ 300
    VIAGNVVTRE QAALLIEAGA DALRIGMGSG SICITQEVMA CGRPQGTAVY 350
    GVTEFANKFG VPCIADGGIG NIGHITKALA LGASCVMMGG LLAGTAETPG 400
    DYFYRDGKRL KTYRGMGSID AMQQTNTNAN ASTSRYFSEA DKVLVAQGVS 450
    GSVVDKGSIT KFVPYLYNGL QHSLQDIGIK SIDELRENVD NGEIRFEFRT 500
    ASAQFEGGVH GLHSYEKRLH N 521
    Length:521
    Mass (Da):56,239
    Last modified:July 1, 1997 - v1
    Checksum:i5F1E52611B1E1418
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U85049 Genomic DNA. Translation: AAB51509.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U85049 Genomic DNA. Translation: AAB51509.1 .

    3D structure databases

    ProteinModelPortali O00086.
    SMRi O00086. Positions 9-519.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5476.CAL0000509.

    2D gel databases

    COMPLUYEAST-2DPAGE O00086.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    CGDi CAL0000509. IMH3.

    Phylogenomic databases

    eggNOGi COG0517.
    PhylomeDBi O00086.

    Enzyme and pathway databases

    UniPathwayi UPA00601 ; UER00295 .

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    HAMAPi MF_01964. IMPDH.
    InterProi IPR013785. Aldolase_TIM.
    IPR000644. CBS_dom.
    IPR005990. IMP_DH.
    IPR015875. IMP_DH/GMP_Rdtase_CS.
    IPR001093. IMP_DH_GMPRt.
    [Graphical view ]
    PANTHERi PTHR11911:SF6. PTHR11911:SF6. 1 hit.
    Pfami PF00571. CBS. 2 hits.
    PF00478. IMPDH. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000130. IMPDH. 1 hit.
    SMARTi SM00116. CBS. 2 hits.
    [Graphical view ]
    TIGRFAMsi TIGR01302. IMP_dehydrog. 1 hit.
    PROSITEi PS51371. CBS. 2 hits.
    PS00487. IMP_DH_GMP_RED. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Overexpression of a cloned IMP dehydrogenase gene of Candida albicans confers resistance to the specific inhibitor mycophenolic acid."
      Koehler G.A., White T.C., Agabian N.
      J. Bacteriol. 179:2331-2338(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ENZYME REGULATION.
      Strain: SS.

    Entry informationi

    Entry nameiIMDH_CANAX
    AccessioniPrimary (citable) accession number: O00086
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: July 1, 1997
    Last modified: October 1, 2014
    This is version 96 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3